Search for dissertations about: "Protein design"

Showing result 1 - 5 of 447 swedish dissertations containing the words Protein design.

  1. 1. Antiadhesive agents targeting uropathogenic Escherichia coli : Multivariate studies of protein-protein and protein-carbohydrate interactions

    Author : Andreas Larsson; Jan Kihlberg; Fredrik Almqvist; Mats Larhed; Umeå universitet; []
    Keywords : NATURAL SCIENCES; NATURVETENSKAP; NATURVETENSKAP; NATURAL SCIENCES; Organic chemistry; Antibacterial; pili; antiadhesive agents; structure based design; statistical molecular design; 2-pyridone; amino acid derivative; galabiose; enaminone; SPR; ELISA; QSAR; Organisk kemi; Organic chemistry; Organisk kemi; organisk kemi; Organic Chemistry;

    Abstract : This thesis describes studies directed towards development of novel antiadhesive agents, with particular emphasis on compounds that prevent attachment of bacteria to a host-cell. Three different proteins involved in the assembly or function of adhesive pili in uropathogenic Escherichia coli have been targeted either by rational structure based design or statistical molecular methods. READ MORE

  2. 2. Protein-protein interactions in model systems : design, control of catalytic activity and biosensor applications

    Author : Johan Rydberg; Lars Baltzer; Joel Schneider; Linköpings universitet; []
    Keywords : NATURAL SCIENCES; NATURVETENSKAP; Chemistry; Protein interactions; design; catalysis; biosensors; hybride materials; nanoparticles; Kemi; Chemistry; Kemi;

    Abstract : This thesis describes the design of polypeptides, unordered in the monomeric state but capable of folding into helix-loop-helix motifs and dimerise to form four-helix bundles. The goal of the design was to encode them with the capacity to form dimers highly selectively and the ability to carry out molecular functions in the folded state but not in the unordered state, and thus to establish a molecular link between recognition and function. READ MORE

  3. 3. Thermodynamics of Protein Folding and Design

    Author : Erik Sandelin; Beräkningsbiologi och biologisk fysik; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; protein folding; hydrophobicity; Monte Carlo; sequence analysis; sequence assembly; shotgun sequencing; Mathematical and general theoretical physics; classical mechanics; quantum mechanics; relativity; gravitation; statistical physics; Matematisk och allmän teoretisk fysik; thermodynamics; termodynamik; Fysicumarkivet A:2000:Sandelin; statistisk fysik; relativitet; protein design; klassisk mekanik; kvantmekanik;

    Abstract : The protein folding and protein design problems are addressed, using coarse-grained models with only two types of amino acids, hydrophobic and hydrophilic. In addition to hydrophobicity forces, the models contain sequence-independent local interactions which are found to strongly influence the thermodynamics of these models. READ MORE

  4. 4. Structure determination and thermodynamic stabilization of an engineered protein-protein complex

    Author : Elisabet Wahlberg; Per-Åke Nygren; Bengt-Harald Jonsson; KTH; []
    Keywords : ENGINEERING AND TECHNOLOGY; TEKNIK OCH TEKNOLOGIER; TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; affibody; protein structure; coupled folding; NMR spectroscopy; protein stability; protein-protein interactions; binding thermodynamics; isothermal titration calorimetry; protein engineering; Structural biochemistry; Strukturbiokemi;

    Abstract : The interaction between two 6 kDa proteins has been investigated. The studied complex of micromolar affinity (Kd) consists of the Z domain derived from staphylococcal protein A and the related protein ZSPA-1, belonging to a group of binding proteins denoted affibody molecules generated via combinatorial engineering of the Z domain. READ MORE

  5. 5. An evolutionary basis for protein design and structure prediction

    Author : Christoffer Norn; Biokemi och Strukturbiologi; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; Protein evolution; Biophysics; Protein design; Protein structure prediction;

    Abstract : The sequence diversity of protein families is a result of the biophysical selection pressures that shaped their evolutionary history. Among the dominant pressures is selection for protein thermostability, which in itself is an attractive target in protein engineering because of its importance for various biopharmaceutical properties, the performance of industrial enzymes, and the ability to design new protein functions. READ MORE